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A resonance Raman band assignable to the O–O stretching mode in the resting oxidized state of bovine heart cytochrome c oxidase

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Abstract

In the resting oxidized state (the fully oxidized “as-isolated” state) of cytochrome c oxidase (CcO) preparation, a resonance Raman band is observed at 755 cm-1 upon 647.1 nm excitation in resonance with an absorption band at 655 nm. Addition of cyanide eliminates the Raman band concomitant with loss of the absorption band at 655 nm. These results strongly suggest that the Raman band at 755 cm-1 originates from the O−O stretching mode of the bridging peroxide (Fe−O-−O-−Cu) in the O2 reduction site of the fully oxidized “as-isolated” CcO. Although the peroxide bridged structure has been proposed on the basis of X-ray crystallography and reductive titration experiments, the present vibrational spectroscopic analyses reveal conclusively the chemical nature of the bridging ligand at the O2 reduction site of the fully oxidized “as-isolated” bovine heart CcO.

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Authors and Affiliations

  1. Picobiology Institute, Department of Life Science, Graduate School of Life Science, University of Hyogo, Koto 3-2-1, Kamigori-cho, Ako-gun, Hyogo, 678-1297, Japan

    Miyuki Sakaguchi, Kyoko Shinzawa-Itoh, Shinya Yoshikawa & Takashi Ogura

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  1. Miyuki Sakaguchi
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  2. Kyoko Shinzawa-Itoh
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  3. Shinya Yoshikawa
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  4. Takashi Ogura
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Correspondence to Takashi Ogura.

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Sakaguchi, M., Shinzawa-Itoh, K., Yoshikawa, S. et al. A resonance Raman band assignable to the O–O stretching mode in the resting oxidized state of bovine heart cytochrome c oxidase. J Bioenerg Biomembr 42, 241–243 (2010). https://doi.org/10.1007/s10863-010-9282-y

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  • DOI: https://doi.org/10.1007/s10863-010-9282-y

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